ID   PLB1_RAT                Reviewed;        1450 AA.
AC   O54728;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Phospholipase B1, membrane-associated;
DE            Short=Phospholipase B;
DE   AltName: Full=Lysophospholipase;
DE            EC=3.1.1.5 {ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065};
DE   AltName: Full=Phospholipase A2;
DE            EC=3.1.1.4 {ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065};
DE   AltName: Full=Phospholipase B/lipase;
DE            Short=PLB/LIP;
DE   AltName: Full=Triacylglycerol lipase;
DE            EC=3.1.1.3 {ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065};
DE   Flags: Precursor;
GN   Name=Plb1; Synonyms=Phlpb;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, PROTEOLYTIC PROCESSING, DOMAIN, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Ileal mucosa;
RX   PubMed=9442065; DOI=10.1074/jbc.273.4.2222;
RA   Takemori H., Zolotaryov F.N., Ting L., Urbain T., Komatsubara T.,
RA   Hatano O., Okamoto M., Tojo H.;
RT   "Identification of functional domains of rat intestinal phospholipase
RT   B/lipase. Its cDNA cloning, expression, and tissue distribution.";
RL   J. Biol. Chem. 273:2222-2231(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 368-380 AND 529-559, FUNCTION, CATALYTIC ACTIVITY,
RP   ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=9442064; DOI=10.1074/jbc.273.4.2214;
RA   Tojo H., Ichida T., Okamoto M.;
RT   "Purification and characterization of a catalytic domain of rat intestinal
RT   phospholipase B/lipase associated with brush border membranes.";
RL   J. Biol. Chem. 273:2214-2221(1998).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=1716922; DOI=10.1139/o91-054;
RA   Pind S., Kuksis A.;
RT   "Further characterization of a novel phospholipase B (phospholipase A2-
RT   lysophospholipase) from intestinal brush-border membranes.";
RL   Biochem. Cell Biol. 69:346-357(1991).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF SER-404;
RP   SER-414; SER-429; SER-459; ASP-518; HIS-659; HIS-665 AND HIS-686.
RX   PubMed=11401559; DOI=10.1021/bi010237n;
RA   Lu T., Ito M., Tchoua U., Takemori H., Okamoto M., Tojo H.;
RT   "Identification of essential residues for catalysis of rat intestinal
RT   phospholipase B/lipase.";
RL   Biochemistry 40:7133-7139(2001).
CC   -!- FUNCTION: Calcium-independent membrane-associated phospholipase that
CC       catalyzes complete diacylation of phospholipids by hydrolyzing both sn-
CC       1 and sn-2 fatty acyl chains attached to the glycerol backbone
CC       (phospholipase B activity) (By similarity). Has dual phospholipase and
CC       lysophospholipase activities toward diacylphospholipids
CC       (PubMed:9442065, PubMed:9442064, PubMed:11401559). Preferentially
CC       cleaves sn-2 ester bonds over sn-1 bonds (PubMed:9442064). Acts as a
CC       lipase toward glycerolipid substrates (PubMed:9442065, PubMed:9442064,
CC       PubMed:11401559). Hydrolyzes fatty acyl chains of diacylglycerols with
CC       preference for the sn-2 position and of triacylglycerols with not
CC       positional selectivity (PubMed:9442065, PubMed:9442064,
CC       PubMed:11401559). May also hydrolyze long chain retinyl esters such as
CC       retinyl palmitate (By similarity). May contribute to digestion of
CC       dietary phospholipids, glycerolipids and retinoids, facilitating lipid
CC       absorption at the brush border (Probable).
CC       {ECO:0000250|UniProtKB:Q05017, ECO:0000269|PubMed:11401559,
CC       ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065,
CC       ECO:0000305|PubMed:9442064}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC         Evidence={ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064,
CC         ECO:0000269|PubMed:9442065};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC         Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064,
CC         ECO:0000305|PubMed:9442065};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC         Evidence={ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064,
CC         ECO:0000269|PubMed:9442065};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC         Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064,
CC         ECO:0000305|PubMed:9442065};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC         H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC         Evidence={ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064,
CC         ECO:0000269|PubMed:9442065};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC         Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064,
CC         ECO:0000305|PubMed:9442065};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC         hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC         Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC         Evidence={ECO:0000269|PubMed:9442064};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC         Evidence={ECO:0000305|PubMed:9442064};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC         + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC         phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC         ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:11401559,
CC         ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC         Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064,
CC         ECO:0000305|PubMed:9442065};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O =
CC         (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC         + H(+); Xref=Rhea:RHEA:40923, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28610, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669;
CC         Evidence={ECO:0000269|PubMed:9442064};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40924;
CC         Evidence={ECO:0000305|PubMed:9442064};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC         phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-
CC         glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC         ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC         Evidence={ECO:0000250|UniProtKB:Q05017};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC         Evidence={ECO:0000250|UniProtKB:Q05017};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC         phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC         phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:40971,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:73002, ChEBI:CHEBI:76084;
CC         Evidence={ECO:0000250|UniProtKB:Q05017};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40972;
CC         Evidence={ECO:0000250|UniProtKB:Q05017};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphoethanolamine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-
CC         glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40911,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:73004, ChEBI:CHEBI:73007;
CC         Evidence={ECO:0000269|PubMed:9442064};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912;
CC         Evidence={ECO:0000305|PubMed:9442064};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC         sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC         3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:72841, ChEBI:CHEBI:75158;
CC         Evidence={ECO:0000269|PubMed:9442064};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC         Evidence={ECO:0000305|PubMed:9442064};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + 2 H2O = 2
CC         H(+) + 2 hexadecanoate + sn-glycerol 3-phosphocholine;
CC         Xref=Rhea:RHEA:40975, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72999;
CC         Evidence={ECO:0000250|UniProtKB:Q05017};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40976;
CC         Evidence={ECO:0000250|UniProtKB:Q05017};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine
CC         + H2O = (9Z)-octadecenoate + 1-O-hexadecyl-sn-glycero-3-
CC         phosphocholine + H(+); Xref=Rhea:RHEA:40915, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:34112,
CC         ChEBI:CHEBI:64496; Evidence={ECO:0000269|PubMed:9442064};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40916;
CC         Evidence={ECO:0000305|PubMed:9442064};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC         hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC         Evidence={ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064,
CC         ECO:0000269|PubMed:9442065};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064,
CC         ECO:0000305|PubMed:9442065};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC         octadecenoate + di-(9Z)-octadecenoylglycerol + H(+);
CC         Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945;
CC         Evidence={ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064,
CC         ECO:0000269|PubMed:9442065};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC         Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064,
CC         ECO:0000305|PubMed:9442065};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol
CC         + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + H(+) +
CC         octadecanoate; Xref=Rhea:RHEA:41111, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75466,
CC         ChEBI:CHEBI:77623; Evidence={ECO:0000269|PubMed:9442064};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41112;
CC         Evidence={ECO:0000305|PubMed:9442064};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = (9Z)-
CC         octadecenoate + 1,3-dihexadecanoylglycerol + H(+);
CC         Xref=Rhea:RHEA:40983, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:75688, ChEBI:CHEBI:77619;
CC         Evidence={ECO:0000269|PubMed:9442064};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40984;
CC         Evidence={ECO:0000305|PubMed:9442064};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = 1-
CC         hexadecanoyl-2-(9Z-octadecenoyl)-glycerol + H(+) + hexadecanoate;
CC         Xref=Rhea:RHEA:40979, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:75585, ChEBI:CHEBI:75688;
CC         Evidence={ECO:0000269|PubMed:9442064};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40980;
CC         Evidence={ECO:0000305|PubMed:9442064};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol
CC         + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-3-octadecanoyl-sn-
CC         glycerol + H(+); Xref=Rhea:RHEA:41103, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77623,
CC         ChEBI:CHEBI:77624; Evidence={ECO:0000269|PubMed:9442064};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41104;
CC         Evidence={ECO:0000305|PubMed:9442064};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol
CC         + H2O = 2-(9Z-octadecenoyl)-3-octadecanoyl-sn-glycerol + H(+) +
CC         hexadecanoate; Xref=Rhea:RHEA:41107, ChEBI:CHEBI:7896,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75558,
CC         ChEBI:CHEBI:77623; Evidence={ECO:0000269|PubMed:9442064};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41108;
CC         Evidence={ECO:0000305|PubMed:9442064};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + H2O =
CC         (9Z,12Z)-octadecadienoate + 1-octadecanoyl-sn-glycerol + H(+);
CC         Xref=Rhea:RHEA:40927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:75550, ChEBI:CHEBI:77097;
CC         Evidence={ECO:0000269|PubMed:9442064};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40928;
CC         Evidence={ECO:0000305|PubMed:9442064};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-
CC         octadecenoate + 1-(9Z-octadecenoyl)-sn-glycerol + H(+);
CC         Xref=Rhea:RHEA:41219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:75757;
CC         Evidence={ECO:0000269|PubMed:9442064};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41220;
CC         Evidence={ECO:0000305|PubMed:9442064};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O = (9Z)-
CC         octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H(+);
CC         Xref=Rhea:RHEA:42604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:75824, ChEBI:CHEBI:75938;
CC         Evidence={ECO:0000269|PubMed:9442064};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42605;
CC         Evidence={ECO:0000305|PubMed:9442064};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC         1-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:39939,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:75342, ChEBI:CHEBI:75735;
CC         Evidence={ECO:0000250|UniProtKB:Q05017};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39940;
CC         Evidence={ECO:0000250|UniProtKB:Q05017};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC         glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q05017};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC         Evidence={ECO:0000250|UniProtKB:Q05017};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC         glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q05017};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492;
CC         Evidence={ECO:0000250|UniProtKB:Q05017};
CC   -!- ACTIVITY REGULATION: Up-regulated by bile acids such as deoxycholate
CC       (PubMed:9442065, PubMed:9442064). Inhibited by diisopropyl
CC       fluorophosphate (PubMed:9442065, PubMed:9442064).
CC       {ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8-9. {ECO:0000269|PubMed:9442064};
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:9442064,
CC       ECO:0000269|PubMed:9442065}; Single-pass type I membrane protein
CC       {ECO:0000255}. Note=Present in the intestinal brush border membranes.
CC   -!- TISSUE SPECIFICITY: Expressed in the ileum mucosa, Paneth cells
CC       spermatocytes, spermatids and sperm (at protein level). Expressed in
CC       the ileum, jejunum, esophagus and testis. {ECO:0000269|PubMed:1716922,
CC       ECO:0000269|PubMed:9442065}.
CC   -!- DOMAIN: Repeat 2 contains the catalytic domain.
CC       {ECO:0000269|PubMed:9442065}.
CC   -!- PTM: Undergoes proteolytic cleavage in the ileum.
CC       {ECO:0000269|PubMed:9442065}.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       Phospholipase B1 subfamily. {ECO:0000305}.
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DR   EMBL; D63648; BAA23813.1; -; mRNA.
DR   RefSeq; NP_620253.1; NM_138898.1.
DR   AlphaFoldDB; O54728; -.
DR   STRING; 10116.ENSRNOP00000057888; -.
DR   SwissLipids; SLP:000000624; -.
DR   CarbonylDB; O54728; -.
DR   GlyCosmos; O54728; 14 sites, No reported glycans.
DR   GlyGen; O54728; 14 sites.
DR   iPTMnet; O54728; -.
DR   PhosphoSitePlus; O54728; -.
DR   PaxDb; 10116-ENSRNOP00000057888; -.
DR   Ensembl; ENSRNOT00000061176.4; ENSRNOP00000057888.4; ENSRNOG00000026037.7.
DR   Ensembl; ENSRNOT00055034761; ENSRNOP00055028181; ENSRNOG00055020289.
DR   Ensembl; ENSRNOT00060022051; ENSRNOP00060017467; ENSRNOG00060012921.
DR   GeneID; 192259; -.
DR   KEGG; rno:192259; -.
DR   AGR; RGD:621565; -.
DR   CTD; 151056; -.
DR   RGD; 621565; Plb1.
DR   eggNOG; KOG3670; Eukaryota.
DR   GeneTree; ENSGT00530000063883; -.
DR   InParanoid; O54728; -.
DR   OMA; FCSDPVH; -.
DR   OrthoDB; 6003at2759; -.
DR   PhylomeDB; O54728; -.
DR   Reactome; R-RNO-1482788; Acyl chain remodelling of PC.
DR   Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR   PRO; PR:O54728; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR   GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IDA:UniProtKB.
DR   GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0004623; F:phospholipase A2 activity; IDA:RGD.
DR   GO; GO:0050253; F:retinyl-palmitate esterase activity; IDA:RGD.
DR   GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR   GO; GO:0046340; P:diacylglycerol catabolic process; IDA:UniProtKB.
DR   GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
DR   GO; GO:0046338; P:phosphatidylethanolamine catabolic process; IDA:UniProtKB.
DR   GO; GO:0034478; P:phosphatidylglycerol catabolic process; IDA:UniProtKB.
DR   GO; GO:0006644; P:phospholipid metabolic process; IDA:RGD.
DR   GO; GO:2000344; P:positive regulation of acrosome reaction; ISO:RGD.
DR   GO; GO:0042572; P:retinol metabolic process; IDA:RGD.
DR   GO; GO:0019433; P:triglyceride catabolic process; IDA:UniProtKB.
DR   CDD; cd01824; Phospholipase_B_like; 4.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 3.
DR   InterPro; IPR001087; GDSL.
DR   InterPro; IPR008265; Lipase_GDSL_AS.
DR   InterPro; IPR035547; Phospholipase_B.
DR   InterPro; IPR038885; PLB1.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   PANTHER; PTHR21325; PHOSPHOLIPASE B, PLB1; 1.
DR   PANTHER; PTHR21325:SF52; PHOSPHOLIPASE B1, MEMBRANE-ASSOCIATED; 1.
DR   Pfam; PF00657; Lipase_GDSL; 3.
DR   SUPFAM; SSF52266; SGNH hydrolase; 3.
DR   PROSITE; PS01098; LIPASE_GDSL_SER; 2.
PE   1: Evidence at protein level;
KW   Cell membrane; Coiled coil; Direct protein sequencing; Glycoprotein;
KW   Hydrolase; Lipid metabolism; Membrane; Phospholipid metabolism;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..1450
FT                   /note="Phospholipase B1, membrane-associated"
FT                   /id="PRO_0000324386"
FT   TOPO_DOM        28..1422
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1423..1443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1444..1450
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          41..351
FT                   /note="1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          366..711
FT                   /note="2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          712..1058
FT                   /note="3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1068..1407
FT                   /note="4"
FT                   /evidence="ECO:0000255"
FT   REGION          41..1407
FT                   /note="4 X 308-326 AA approximate repeats"
FT                   /evidence="ECO:0000255"
FT   REGION          708..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1408..1450
FT                   /note="Necessary for membrane localization"
FT                   /evidence="ECO:0000269|PubMed:9442065"
FT   ACT_SITE        404
FT                   /evidence="ECO:0000305|PubMed:11401559"
FT   ACT_SITE        518
FT                   /evidence="ECO:0000305|PubMed:11401559"
FT   ACT_SITE        659
FT                   /evidence="ECO:0000305|PubMed:11401559"
FT   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        699
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        787
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        801
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        844
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        880
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        926
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1059
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1383
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   MUTAGEN         404
FT                   /note="S->A,C: Loss of PLA2, lysophospholipase and lipase
FT                   activities."
FT                   /evidence="ECO:0000269|PubMed:11401559"
FT   MUTAGEN         414
FT                   /note="S->A: No effect on lysophospholipase to PLA2
FT                   activity ratio."
FT                   /evidence="ECO:0000269|PubMed:11401559"
FT   MUTAGEN         429
FT                   /note="S->A: No effect on activity."
FT                   /evidence="ECO:0000269|PubMed:11401559"
FT   MUTAGEN         459
FT                   /note="S->A: Decrease in PLA2, lysophospholipase and lipase
FT                   activities."
FT                   /evidence="ECO:0000269|PubMed:11401559"
FT   MUTAGEN         518
FT                   /note="D->A,V: Loss of PLA2, lysophospholipase and lipase
FT                   activities."
FT                   /evidence="ECO:0000269|PubMed:11401559"
FT   MUTAGEN         518
FT                   /note="D->E,N: Impairs PLA2, lysophospholipase and lipase
FT                   activities."
FT                   /evidence="ECO:0000269|PubMed:11401559"
FT   MUTAGEN         659
FT                   /note="H->A: Loss of PLA2, lysophospholipase and lipase
FT                   activities."
FT                   /evidence="ECO:0000269|PubMed:11401559"
FT   MUTAGEN         665
FT                   /note="H->A: Impairs PLA2, lysophospholipase and lipase
FT                   activities."
FT                   /evidence="ECO:0000269|PubMed:11401559"
FT   MUTAGEN         686
FT                   /note="H->A: No effect on activity."
FT                   /evidence="ECO:0000269|PubMed:11401559"
SQ   SEQUENCE   1450 AA;  161089 MW;  4555898C8FD91F45 CRC64;
     MESWPGVSLV GLLLLLLLGQ GPSQIHGSSG ENTSQPQQVF RTLKNFSFPC KPKKLELSVL
     SKSVHSLRPS DIKLVAAIGN LETPPAPGSG VVNMEKPQSL ESELQNVCIG IMTALSDIIR
     HFNPSVLMPT CSPGKGTAGH TTIAEDLWIQ AKELVRHLKD NPELDFEKDW KLITVLFSNT
     SQCHLCSSDQ QKRHLMKHME MLSGVLDYLH REVPRAFVNL VDLSEVLTMA QQHQETGFSP
     APEICKCSEE ITKLSKAVMQ WSYQEAWEDL LASSKFNKHE TFAVVFQSFF SEVELPLERP
     SPQDSTTLAL RIWNSMMEPV GRKDGTLNEA ERKTMKCPSQ ESPYLFTYRN SNYQARQLKP
     IGKFQMKEGT KFTCPDKDPS DSIPTTVHRL RPADIKVIGA MGDSLTAGNG AGSSPGNVLD
     VLTQYRGLSW SVGGDETIET VTTLANILRE FNPSLKGFSV GTGKENTPRA SFNQAVAGAK
     SDGLAAQAKK LVSLMKDDKT INFQEDWKII TVFIGGNDLC GSCNNLARFS PQTFTDNIKT
     ALDILHAEVP RAFVNMVSVI EITPLRELFN EPKVSCPRMI LRSLCPCVLN LGENSAELAQ
     LVERNRQYQE ETGKLIESGR YDTRDDFTVV LQPMFENVVM PRTLEGLPDS SFFAPDCFHF
     NVKTHARSAI ALWKNMLEPV GRKTRHQNFE IKVPIMCPNQ TSPFLSTTKN SNLGHGTSMS
     CEEKAPSASP PTSVHTLRPA DIQVVAALGD SVTAGNGISS QEGDLADVTT QYRGLSYSAG
     GDKFLENVTT LPNILREFNG NLTGYSVGTG DVNSASAFLN QAVPGAKAEN LASQVQTLIQ
     KMKNDTRVNF HQDWKVITVM IGASDLCDFC KDSNRYSAAN FSDHLRNALD ILHKEVPRAL
     VNLVDFMNPS IIRQVFLKNP DKCPVNQTSV LCNCVLTPGE DSHELARLEA FTKSYQSSML
     QLVESGRYDT REDFSVVLQP FLFNIRLPIL ENGNPDTSFF APDCILLSQK FHTQLARALW
     ANMLEPLGKK MDTLDPKELI ALACPTKDKP FLRTFRNSNY TYPIKPAIEN WGSDFLCTEQ
     SPSSKVPTSV HELRPSDIKV VAAMGDFLTT ATGARPSESS SLDTPWRGLS WSIGGDGTLE
     THTTLPNILK KFNPSILGFS TGTLENTAGL NVAEEGARAQ DMPAQAQALV KKMKSTPTIN
     IQEDWKLITL LIGNNDLCLY CEDPENYSTR EYVKYIQHAL DIFYEELPRV FINVVEVMEL
     SGLLHDQGGK CAMPLAVQKN CSCLKRSQNL MAMQELKKVN GNLQSALSEL SYWHRYMQRE
     DFAVTVQPFF RNTFVPLDER GGLDLTFFSE DCFHFSVRGH AEMAIALWNN MLEPVGKKTT
     SNNFTYNRTK LKCPSPENPF LYTVRNSQIL LDKAKENSNT LYWAVPVAAV GGLVVGILGM
     MLWRTVRLVQ
//